Molecular & Cellular Proteomics
ResearchIntegrated Omics and Computational Glycobiology Reveal Structural Basis for Influenza A Virus Glycan Microheterogeneity and Host Interactions*
Cited by (0)
Author contributions: Study design and direction: JZ, KLH. Omics data acquisition: KK, NL. Data analysis: KK, JAK. Bioassays: MRW, KK. Molecular modeling design: RJW. Modeling: OCG.
- *
This work was supported by NIH grants P41GM104603 (JZ, KK, JAK), NIH R01 GM100058, and P41 GM103390 (OCG, RJW) and R01 HL069031 (KLH and MRW). D.F. Smith and R.D. Cummings carried out the CFG glycan array analyses at the National Center for Functional Glycomics (Emory University School of Medicine) funded by the NIH grant P41GM103694. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
This article contains supplemental material.
- 1
The abbreviations used are:
- IAV
Influenza A virus
- CAD
Collision-activated dissociation
- D+R
NCRD with two amino acid mutations
- ERManI
Endoplasmic reticulum class I α-mannosidase
- HA
Hemagglutinin
- HCD
Higher-energy collisional dissociation
- HILIC
Hydrophilic-interaction liquid chromatography
- huNCRD
Wild-type human neck and carbohydrate recognition domain of SP-D
- LC-MS
Liquid chromatography-mass spectrometry
- MD
Molecular Dynamics
- MS/MS
Tandem mass spectrometry
- MS2
Tandem mass spectrometry
- Phil-82
A/Philippines/2/1982 (H3N2)
- Phil-BS
A/Philippines/2/1982/BS (H3N2) (Bovine serum escape mutant)
- PR-08
A/Puerto Rico/8/1934 (H1N1)
- PTM
Post-translational modification
- R343V
NCRD with single amino acid mutation
- rhSPDII
Recombinant full length human SP-D
- SP-D
Surfactant protein-D.